STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ybaKPutative DNA-dependent transcriptional regulator,YbaK.68% identity (75% similarity) to TrEMBL;Q748B9. TrEMBL; Q8FK79(29% identity to E.coli,ybaK).SwissProt;P37175 Has PF04073, YbaK / prolyl-tRNA synthetases associated domain;IPR007214; This domain of unknown function is found in numerous prokaryote organisms. The structure of YbaK shows a novel fold. This domain also occurs in a number of prolyl-tRNA synthetases (proRS) from prokaryotes. Thus, the domain is thought to be involved in oligo-nucleotide binding, with possible roles in recognition/discrimination or editing of prolyl-tRNA. T [...] (163 aa)    
Predicted Functional Partners:
xerD
Integrase/recombinase; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.
       0.743
azo2479
Conserved hypothetical membrane protein. Homology to VV12384 of Vibrio vulnificus of 60% (trembl|Q8DA26). No domains predicted. TMHMM2 reporting 1 TMH present. No signal peptide present; Conserved hypothetical protein.
    
   0.715
fliE
Flagellar hook-basal body complex protein FliE; Region start changed from 2997519 to 2997495 (-24 bases).
    
   0.715
fliN
Flagellar motor switch protein fliN (Flagellar motor switch protein mopA) (Fragment). FliN is one of three proteins (FliG FliN FliM) that form a switch complex that is proposed to be located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins in addition to contacting components of the motor that determine the dirction of flagellar rotation (by similarity). InterPro: Surface presentation of antigens (SPOA) protein, Flagellar motor switch FliN protein Pfam: Surface presentation of antigens (SPOA) protein no signal peptide no TMHs; High confid [...]
    
   0.715
flgD
Probable basal-body rod modification protein FlgD; Required for flagellar hook formation. May act as a scaffolding protein.
    
   0.715
cheR1
Probable chemotaxis protein methyltransferase; Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
    
   0.612
cheR2
Chemotaxis protein methyltransferase; Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
    
   0.612
flgG
Flagellar basal-body rod protein flgG (Distal rod protein). The rod has been shown to consist of four different, yet evolutionary related proteins: in the distal portion of the rod there are about 26 subunits of protein flgG and in the proximal portion there are about six subunits each of proteins flgB, flgC, and flgF. These four proteins contain a highly conserved asparagine-rich domain at their N terminus. InterPro: Flagella basal body rod protein no signal peptide no TMHs; High confidence in function and specificity.
    
   0.612
proS
Proline--tRNA ligase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...]
     
 0.545
aspS
AspS protein; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
    
 0.496
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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